[Incorporation of Copper Ions into T2/T3 Centers of Two-Domain Laccases].

Autor:	Gabdulkhakov AG; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Kostareva OS; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Kolyadenko IA; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Mikhaylina AO; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Trubitsina LI; Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Tishchenko SV; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.; sveta@vega.protres.ru.
Jazyk:	ruština
Zdroj:	Molekuliarnaia biologiia [Mol Biol (Mosk)] 2018 Jan-Feb; Vol. 52 (1), pp. 29-35.
DOI:	10.7868/S0026898418010056
Abstrakt:	Laccase belongs to the family of copper-containing oxidases. A study was made of the mechanism that sustains the incorporation of copper ions into the T2/T3 centers of recombinant two-domain laccase Streptomyces griseoflavus Ac-993. The occupancy of the T3 center by copper ions was found to increase with an increasing copper content in the culture medium and after dialysis of the protein preparation against a copper sulfate-containing buffer. The T2 center was filled only when overproducer strain cells were grown at a higher copper concentration in the medium. Two-domain laccases were assumed to possess a channel that serves to deliver copper ions to the T3 center during the formation of the three-dimensional laccase conformation and dialysis of the protein preparation. A narrower channel leads to the T2 center in two-domain laccases compared with three-domain ones, rendering the center less accessible for copper atoms. The incorporation of copper ions into the T2 center of two-domain laccases is likely to occur in the course of their biosynthesis or the formation of a functional trimer.
Databáze:	MEDLINE
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